Literature DB >> 17998541

Structure of PlcR: Insights into virulence regulation and evolution of quorum sensing in Gram-positive bacteria.

Nathalie Declerck1, Laurent Bouillaut, Denis Chaix, Nathalie Rugani, Leyla Slamti, François Hoh, Didier Lereclus, Stefan T Arold.   

Abstract

Gram-positive bacteria use a wealth of extracellular signaling peptides, so-called autoinducers, to regulate gene expression according to population densities. These "quorum sensing" systems control vital processes such as virulence, sporulation, and gene transfer. Using x-ray analysis, we determined the structure of PlcR, the major virulence regulator of the Bacillus cereus group, and obtained mechanistic insights into the effects of autoinducer binding. Our structural and phylogenetic analysis further suggests that all of those quorum sensors that bind directly to their autoinducer peptide derive from a common ancestor and form a single family (the RNPP family, for Rap/NprR/PlcR/PrgX) with conserved features. As a consequence, fundamentally different processes in different bacterial genera appear regulated by essentially the same autoinducer recognition mechanism. Our results shed light on virulence control by PlcR and elucidate origin and evolution of multicellular behavior in bacteria.

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Year:  2007        PMID: 17998541      PMCID: PMC2141804          DOI: 10.1073/pnas.0704501104

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  37 in total

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Review 5.  Quorum sensing: cell-to-cell communication in bacteria.

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  66 in total

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3.  Bacillus subtilis RapA phosphatase domain interaction with its substrate, phosphorylated Spo0F, and its inhibitor, the PhrA peptide.

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6.  Diversity of the Rap-Phr quorum-sensing systems in the Bacillus cereus group.

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7.  Rap Protein Paralogs of Bacillus thuringiensis: a Multifunctional and Redundant Regulatory Repertoire for the Control of Collective Functions.

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8.  Efficacy of vitrectomy in improving the outcome of Bacillus cereus endophthalmitis.

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10.  Structural basis for the activation mechanism of the PlcR virulence regulator by the quorum-sensing signal peptide PapR.

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